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Thursday, December 22, 2011

Satellite short course to the Sixth International Meeting of the Latin American Society for Developmental Biology, April 16-25, 2012, Montevideo, Uruguay. This Pan-American Advanced Studies Institute will be held at the Universidad de la Republica and Institut Pasteur de Montevideo and is funded by a PASI program grant from NSF and DoE. It is aimed for advanced graduate students, postdoctoral fellows and junior faculty interested in enhancing their understanding for evolutionary processes by integrating genomics, systems biology, gene regulatory network with traditional experimental approaches. Latin American citizens, US nationals and permanent residents are invited to apply. Deadline for submission is January 6, 2012, 6 PM Eastern time. URL: http://www.sdbonline.org/2012Course/course.htm

Thursday, December 15, 2011

Fifty years after the pioneering discovery hat a protein's three-dimensional structure is determined solely by the sequence of its amino acids, an international team of researchers has taken a major step toward fulfilling the tantalizing promise: predicting the structure of a protein from its DNA alone.

In molecular biology and biomedical engineering, knowing the shape of protein molecules is key to understanding how they perform the work of life, the mechanisms of disease and drug design. Normally the shape of protein molecules is determined by expensive and complicated experiments, and for most proteins these experiments have not yet been done. Computing the shape from genetic information alone is possible in principle. But despite limited success for some smaller proteins, this challenge has remained essentially unsolved. The difficulty lies in the enormous complexity of the search space, an astronomically large number of possible shapes. Without any shortcuts, it would take a supercomputer many years to explore all possible shapes of even a small protein.

The team tested this hypothesis: That evolution can provide a roadmap to how the protein folds. Their approach combined three key elements: evolutionary information accumulated for many millions of years; data from high-throughput genetic sequencing; and a key method from statistical physics.

Using the accumulated evolutionary information in the form of the sequences of thousands of proteins, grouped in protein families that are likely to have similar shapes, the team found a way to solve the problem: an algorithm to infer which parts of a protein interact to determine its shape. They used a principle from statistical physics called "maximum entropy" in a method that extracts information about microscopic interactions from measurement of system properties.

With these internal protein interactions inhand, widely used molecular simulation software generated the atomic details of the protein shape. The team was for the first time able to compute remarkably accurate shapes from sequence information alone for a test set of 15 diverse proteins, with no protein size limit in sight, with unprecedented accuracy.

To test their method, the researchers initially focused on the Ras family of signaling proteins, which has been extensivelystudied because of its known link to cancer. The structure of several Ras-type proteins has already been solved experimentally, but the proteins in the family are larger–with about 160 amino acid residues–than any proteinsmodeled computationally from sequence alone. And there is no reason that the method couldn't work with even larger proteins.

The researchers caution that there are other limits, however: experimental structures, when available, generally are more accurate in atomic detail. And, the method works only when researchers havegenetic data for large protein families. But advances in DNA sequencing have yielded a torrent of such data that is forecast to continue growing exponentially in the foreseeable future.

The next step, the researchers say, is to predict the structures of unsolved proteins currently being investigated bystructural biologists, before exploring the large uncharted territory of currently unknown protein structures; and, collaborating with computational and experimental structural biologists to further refine the "evfolded" proteins and to make structure determination more efficient.

Adapted from text by R Alan Leo, Harvard Medical School.

A full news report: http://www.sciencedaily.com/releases/2011/12/111207175635.htm